ID A0A010S8K5_9PEZI Unreviewed; 1666 AA.
AC A0A010S8K5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase {ECO:0000256|ARBA:ARBA00012900};
DE EC=1.14.11.66 {ECO:0000256|ARBA:ARBA00012900};
GN ORFNames=CFIO01_10464 {ECO:0000313|EMBL:EXF81018.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF81018.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF81018.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF81018.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA-
CC COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961;
CC EC=1.14.11.66; Evidence={ECO:0000256|ARBA:ARBA00000040};
CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00009711}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXF81018.1}.
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DR EMBL; JARH01000404; EXF81018.1; -; Genomic_DNA.
DR RefSeq; XP_007595319.1; XM_007595257.1.
DR STRING; 1445577.A0A010S8K5; -.
DR KEGG; cfj:CFIO01_10464; -.
DR eggNOG; KOG0958; Eukaryota.
DR eggNOG; KOG1080; Eukaryota.
DR HOGENOM; CLU_001442_4_0_1; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000020467; Unassembled WGS sequence.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15571; ePHD; 1.
DR Gene3D; 2.60.120.650; Cupin; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF7; LYSINE-SPECIFIC DEMETHYLASE 4B-RELATED; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 100..141
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 389..552
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 641..764
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1238..1367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1379..1650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..598
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1545
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1549..1607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1666 AA; 184284 MW; 5D6C4FFBDA94D00E CRC64;
MSTDAVSAPV SEPAPVPAQS TTGDHDEEPT LGQIECAKPA FLHSPPDSNN APKSEASDSE
LSDLDDDAVD PSAAPTTQDE APPPEDDIGE VLPDHWSGTV PVFRPTMHQF KDFKLFMTKV
DHYGMKSGIV KIIPPPEWKE NLPRLDDLVK QIRVREPIKQ DIMGSNGTYR QVNILHQRSY
NLPQWRQLCD QSEHQPPARR GERRANVEKP KPRSAPKPRT EAKSTPAGSR KRGRGRPRRG
KAKGKNQDDD DEAEEEQEEE KRPMTPVSPK PAADADVKLK VKKEEVVDSV EDPGLDVDED
EPPTVGRMGR MGGTRQAKPK TQTVSARRKY SKREGSAMID EKAFEDFDYQ MDVSDYTPER
CEELERIYWK TLTYAPPLYG ADLMGTLFDE STEMWNLNKL PNLLDVLGTK VPGVNTAYLY
LGMWKATFAW HLEDVDLYSI NYLHFGAPKQ WYSISQADAR RFEAAMKNIW PTDAKACDQF
LRHKGFLISP SHLKQHYNIT VNKCVSYPGE FVVTYPYGYH SGYNLGYNCA EAVNFALDSW
LPMGKIAKRC ECAQAQDSVW VDVYDIERKL RGEPTPEYEE TDEEDEEDDE DEDEDDATGL
PSPPGSNGIV KSARKRKRAA GDKEGKAKTK RIRLKVKTRA EPTCCLCPSD IPGAEVLPTD
DGRKAHRMCA LYLPETYIDT VDDKEVIANV ANINKERLDL KCLYCRSKKG ACFQCSQKKC
ARAYHATCAA AAGVFVEEAE VPVFGEDGTE YKEQAFEFSC RFHRTKRDRK HTGDSLEDDV
RIREAAAALT KSDICQLQYF KGDIFAGVVV ENRADEQMLL LDIIPNGDRL EVEWKWLLLP
DPSDYHLPKA SSKAIPMPSS QKAKERLNAK RPADEIPRKD APFVEGYTWA EFHPCNECTN
PNQTKVDLSK DSQVWHYLGK TSTEAKAQYS EDPAKQLHNP KSNFLDTIPK PPKPVSASTS
HRRVSVVPPQ PAPLPVFTPG VAVQNGPKSE KPYVYKPRKP VETNYVGTGS FTTQKFTPKA
SAPPTPGGQQ LHFGADPRYP IPGTQFVQQK FAPDVHQQYA PRPAPAGQGY YAAPNSMQRP
SPYSTPGPQP AVGARPAQQT WSTPSQNSRP PLPHSTSQSS TQQNHRRYSA APTPSVAMKY
AFFQVHHNRD SKTYRTPYAP WGGFTNGYEG NLRAHLMRTS PEAFFKNRQG SAQGGTPTPA
PSTGPQGPAY GGPYHNTLTN VMPQGSIGMY GVKTAAPYSS PAPQISQNHA RTPSYSSISP
PPAPGSSRPS SHGQSQGWHA QQPQSAPLHP AIRPQYGGWA NQPQQQPQHP QPAQYQPSQQ
PIPQQTPQQT PQQSPASQPQ STQTKPQHTA KPAVPKVQYK IPEKQTPVPL PAKYLAAMSK
MPSAATPSKA SSKSTSASVQ GTNLPPASHP GKDATQDTST AAVKGSSAQT PSEASKSAGP
TTETAPPVAQ ASVSVPHTPV LAPTSRMPFT NQSMTTAFPR QPTQSQPQAY NMPSTQPLPP
ASRPRTEHLN PAELLAQFAL TPRVNPPTPT APSHQSIPSP VPPQTAAMPG YQNHGSNRGP
TQQQQHQHSQ QPQAWAPPPG QWQPQHHQQY HQHPPLQQYQ QHYQQQNPQQ QPPPPPQQQH
QMQAQPSLPP PHQTPEGDVP LPDVPADSTA LVERMMQNLR RAAFQG
//
